KAD_BURP1
ID KAD_BURP1 Reviewed; 220 AA.
AC Q3JVB1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235};
GN OrderedLocusNames=BURPS1710b_1080;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-215.
RX PubMed=20331978; DOI=10.1016/j.bbrc.2010.03.112;
RA Buchko G.W., Robinson H., Abendroth J., Staker B.L., Myler P.J.;
RT "Structural characterization of Burkholderia pseudomallei adenylate kinase
RT (Adk): profound asymmetry in the crystal structure of the 'open' state.";
RL Biochem. Biophys. Res. Commun. 394:1012-1017(2010).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00235,
CC ECO:0000305|PubMed:20331978}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; CP000124; ABA49610.1; -; Genomic_DNA.
DR RefSeq; WP_004185840.1; NC_007434.1.
DR PDB; 3GMT; X-ray; 2.10 A; A/B=1-215.
DR PDBsum; 3GMT; -.
DR AlphaFoldDB; Q3JVB1; -.
DR SMR; Q3JVB1; -.
DR EnsemblBacteria; ABA49610; ABA49610; BURPS1710b_1080.
DR GeneID; 56594750; -.
DR KEGG; bpm:BURPS1710b_1080; -.
DR HOGENOM; CLU_032354_1_2_4; -.
DR OMA; FHNRMRV; -.
DR OrthoDB; 1491686at2; -.
DR UniPathway; UPA00588; UER00649.
DR EvolutionaryTrace; Q3JVB1; -.
DR Proteomes; UP000002700; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..220
FT /note="Adenylate kinase"
FT /id="PRO_1000058802"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:20331978"
FT REGION 122..159
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:20331978"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 85..88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 132..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 156
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3GMT"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3GMT"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 90..98
FT /evidence="ECO:0007829|PDB:3GMT"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:3GMT"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:3GMT"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3GMT"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:3GMT"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3GMT"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3GMT"
FT HELIX 161..188
FT /evidence="ECO:0007829|PDB:3GMT"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:3GMT"
SQ SEQUENCE 220 AA; 24170 MW; 1AC46DC4D7ECF64F CRC64;
MRLILLGAPG AGKGTQANFI KEKFGIPQIS TGDMLRAAVK AGTPLGVEAK TYMDEGKLVP
DSLIIGLVKE RLKEADCANG YLFDGFPRTI AQADAMKEAG VAIDYVLEID VPFSEIIERM
SGRRTHPASG RTYHVKFNPP KVEGKDDVTG EPLVQRDDDK EETVKKRLDV YEAQTKPLIT
YYGDWARRGA ENGLKAPAYR KISGLGAVEE IRARVFDALK
